Peptide display on functional tailspike protein of bacteriophage P22

X. Carbonell, A. Villaverde

Research output: Contribution to journalArticleResearchpeer-review

9 Citations (Scopus)

Abstract

The tailspike protein (TSP) of Salmonella typhimurium P22 bacteriophage is a multifunctional homotrimer, 6 copies of which are non-covalently attached to the capsid to form the virion tail in the last reaction of phage assembly. An antigenic peptide of foot-and-mouth disease virus (FMDV), aa 134-156 of protein VP1, has been joined to the carboxy terminus of TSP, and produced as a fusion protein in Escherichia coli directed by the trp promoter. The resulting fusion protein is soluble, stable, non-toxic, and can be easily purified by standard procedures. Moreover, both the endorhamnosidase and capsid assembly activities of the TSP are conserved, permitting the fusion protein to reconstitute infectious viruses by in vitro association with tailless particles. In both free TSP and P22 chimeric virions, the foreign peptide is solvent-exposed and highly antigenic, indicating that P22 TSP could be an appropriate carrier protein for multimeric peptide display.
Original languageEnglish
Pages (from-to)225-229
JournalGene
Volume176
Issue number1-2
DOIs
Publication statusPublished - 17 Oct 1996

Keywords

  • Antigenic site
  • Chimeric virus
  • FMDV
  • Neutralization
  • Recombinant protein

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